3P0V
anti-EGFR/HER3 Fab DL11 alone
Summary for 3P0V
| Entry DOI | 10.2210/pdb3p0v/pdb |
| Related | 3P0Y 3P11 |
| Descriptor | Fab DL11 light chain, Fab DL11 heavy chain, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | beta-sandwich, immune system, antigens egfr and her3 |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 94933.50 |
| Authors | Eigenbrot, C.,Shia, S. (deposition date: 2010-09-29, release date: 2011-10-19, Last modification date: 2024-11-27) |
| Primary citation | Schaefer, G.,Haber, L.,Crocker, L.M.,Shia, S.,Shao, L.,Dowbenko, D.,Totpal, K.,Wong, A.,Lee, C.V.,Stawicki, S.,Clark, R.,Fields, C.,Lewis Phillips, G.D.,Prell, R.A.,Danilenko, D.M.,Franke, Y.,Stephan, J.P.,Hwang, J.,Wu, Y.,Bostrom, J.,Sliwkowski, M.X.,Fuh, G.,Eigenbrot, C. A two-in-one antibody against HER3 and EGFR has superior inhibitory activity compared with monospecific antibodies. Cancer Cell, 20:472-486, 2011 Cited by PubMed Abstract: Extensive crosstalk among ErbB/HER receptors suggests that blocking signaling from more than one family member may be essential to effectively treat cancer and limit drug resistance. We generated a conventional IgG molecule MEHD7945A with dual HER3/EGFR specificity by phage display engineering and used structural and mutational studies to understand how a single antigen recognition surface binds two epitopes with high affinity. As a human IgG1, MEHD7945A exhibited dual action by inhibiting EGFR- and HER3-mediated signaling in vitro and in vivo and the ability to engage immune effector functions. Compared with monospecific anti-HER antibodies, MEHD7945A was more broadly efficacious in multiple tumor models, showing that combined inhibition of EGFR and HER3 with a single antibody is beneficial. PubMed: 22014573DOI: 10.1016/j.ccr.2011.09.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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